ID   PDC1_KLUMA              Reviewed;         564 AA.
AC   P33149;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Pyruvate decarboxylase;
DE            EC=4.1.1.1;
GN   Name=PDC1;
OS   Kluyveromyces marxianus (Yeast) (Candida kefyr).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=4911;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8221939; DOI=10.1007/bf00351804;
RA   Holloway P., Subden R.E.;
RT   "The isolation and nucleotide sequence of the pyruvate decarboxylase gene
RT   from Kluyveromyces marxianus.";
RL   Curr. Genet. 24:274-277(1993).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2-oxocarboxylate + H(+) = an aldehyde + CO2;
CC         Xref=Rhea:RHEA:11628, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:17478, ChEBI:CHEBI:35179; EC=4.1.1.1;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + pyruvate = acetaldehyde + CO2; Xref=Rhea:RHEA:45484,
CC         ChEBI:CHEBI:15343, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526; Evidence={ECO:0000250|UniProtKB:P06169};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P06169};
CC       Note=Binds 1 Mg(2+) per subunit. {ECO:0000250|UniProtKB:P06169};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000250|UniProtKB:P06169};
CC       Note=Binds 1 thiamine pyrophosphate per subunit.
CC       {ECO:0000250|UniProtKB:P06169};
CC   -!- SUBUNIT: Homotetramer.
CC   -!- SIMILARITY: Belongs to the TPP enzyme family. {ECO:0000305}.
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DR   EMBL; L09727; AAA35267.1; -; Genomic_DNA.
DR   PIR; S36363; S36363.
DR   AlphaFoldDB; P33149; -.
DR   SMR; P33149; -.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0004737; F:pyruvate decarboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR   InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR   InterPro; IPR000399; TPP-bd_CS.
DR   InterPro; IPR012110; TPP_enzyme.
DR   InterPro; IPR011766; TPP_enzyme-bd_C.
DR   PANTHER; PTHR43452; PTHR43452; 1.
DR   Pfam; PF02775; TPP_enzyme_C; 1.
DR   Pfam; PF00205; TPP_enzyme_M; 1.
DR   Pfam; PF02776; TPP_enzyme_N; 1.
DR   PIRSF; PIRSF036565; Pyruvt_ip_decrb; 1.
DR   SUPFAM; SSF52467; SSF52467; 1.
DR   SUPFAM; SSF52518; SSF52518; 2.
DR   PROSITE; PS00187; TPP_ENZYMES; 1.
PE   3: Inferred from homology;
KW   Decarboxylase; Lyase; Magnesium; Metal-binding; Thiamine pyrophosphate.
FT   CHAIN           1..564
FT                   /note="Pyruvate decarboxylase"
FT                   /id="PRO_0000090766"
FT   BINDING         28
FT                   /ligand="pyruvate"
FT                   /ligand_id="ChEBI:CHEBI:15361"
FT                   /ligand_note="ligand shared between two neighboring
FT                   subunits"
FT                   /evidence="ECO:0000250|UniProtKB:P06169"
FT   BINDING         115
FT                   /ligand="pyruvate"
FT                   /ligand_id="ChEBI:CHEBI:15361"
FT                   /ligand_note="ligand shared between two neighboring
FT                   subunits"
FT                   /evidence="ECO:0000250|UniProtKB:P06169"
FT   BINDING         390
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000250|UniProtKB:P06169"
FT   BINDING         413..415
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000250|UniProtKB:P06169"
FT   BINDING         444
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P06169"
FT   BINDING         445..446
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000250|UniProtKB:P06169"
FT   BINDING         471..476
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000250|UniProtKB:P06169"
FT   BINDING         471
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P06169"
FT   BINDING         473
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P06169"
FT   BINDING         477
FT                   /ligand="pyruvate"
FT                   /ligand_id="ChEBI:CHEBI:15361"
FT                   /ligand_note="ligand shared between two neighboring
FT                   subunits"
FT                   /evidence="ECO:0000250|UniProtKB:P06169"
SQ   SEQUENCE   564 AA;  61901 MW;  1DFDF32840CC88E1 CRC64;
     MSEITLGRYL FERLKQVEVQ TIFGLPGDFN LSLLDKIYEV PGMRWAGNAN ELNAAYAADG
     YARLKGMACV ITTFGVGELS ALNGIAGSYA EHVGVLHVVG VPSISSQAKQ LLLHHTLGNG
     DFTVFHRMSS NISETTAMIT DINSAPSEID RCIRTTYISQ RPVYLGLPAN LVDLKVPASL
     LETPIDLSLK PNDPEAENEV LETVLELIKD AKNPVILADA CCSRHNVKAE TKKLIDITQF
     PAFVTPMGKG SIDEQHPRFG GVYVGTLSSP EVKEAVESAD LVLSVGALLS DFNTGSFSYS
     YKTKNIVEFH SDYIKVRNAT FPGVQMKFVL QKLLTKVKDA AKGYKPVPVP HAPRDNKPVA
     DSTPLKQEWV WTQVGKFLQE GDVVLTETGT SAFGINQTHF PNDTYGISQV LWGSIGFTGG
     ATLGAAFAAE EIDPKKRVIL FIGDGSLQLT VQEISTMIRW GLKPYLFVLN NDGYTIERLI
     HGETAQYNCI QSWKHLDLLP TFGAKDYEAV RVATTGEWNK LTTDKKFQEN SKIRLIEVML
     PVMDAPSNLV KQAQLTASIN AKQE